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Title: Structure of p300 bound to MEF2 on DNA reveals a mechanism of enhanceosome assembly

Authors:
; ; ; ; ; ; ;  [1];  [2];  [2]
  1. USC
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NSFNIHFOREIGN
OSTI Identifier:
1227485
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nucleic Acids Research; Journal Volume: 39; Journal Issue: (10) ; 2011
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

He, Ju, Ye, Jun, Cai, Yongfei, Riquelme, Cecilia, Liu, Jun O., Liu, Xuedong, Han, Aidong, Chen, Lin, Xiamen), and JHU-MED). Structure of p300 bound to MEF2 on DNA reveals a mechanism of enhanceosome assembly. United States: N. p., 2016. Web. doi:10.1093/nar/gkr030.
He, Ju, Ye, Jun, Cai, Yongfei, Riquelme, Cecilia, Liu, Jun O., Liu, Xuedong, Han, Aidong, Chen, Lin, Xiamen), & JHU-MED). Structure of p300 bound to MEF2 on DNA reveals a mechanism of enhanceosome assembly. United States. doi:10.1093/nar/gkr030.
He, Ju, Ye, Jun, Cai, Yongfei, Riquelme, Cecilia, Liu, Jun O., Liu, Xuedong, Han, Aidong, Chen, Lin, Xiamen), and JHU-MED). 2016. "Structure of p300 bound to MEF2 on DNA reveals a mechanism of enhanceosome assembly". United States. doi:10.1093/nar/gkr030.
@article{osti_1227485,
title = {Structure of p300 bound to MEF2 on DNA reveals a mechanism of enhanceosome assembly},
author = {He, Ju and Ye, Jun and Cai, Yongfei and Riquelme, Cecilia and Liu, Jun O. and Liu, Xuedong and Han, Aidong and Chen, Lin and Xiamen) and JHU-MED)},
abstractNote = {},
doi = {10.1093/nar/gkr030},
journal = {Nucleic Acids Research},
number = (10) ; 2011,
volume = 39,
place = {United States},
year = 2016,
month = 7
}
  • No abstract prepared.
  • Herpes simplex virus type-1 expresses a heterodimeric Fc receptor, gE-gI, on the surfaces of virions and infected cells that binds the Fc region of host immunoglobulin G and is implicated in the cell-to-cell spread of virus. gE-gI binds immunoglobulin G at the basic pH of the cell surface and releases it at the acidic pH of lysosomes, consistent with a role in facilitating the degradation of antiviral antibodies. Here we identify the C-terminal domain of the gE ectodomain (CgE) as the minimal Fc-binding domain and present a 1.78-{angstrom} CgE structure. A 5-{angstrom} gE-gI/Fc crystal structure, which was independently verified bymore » a theoretical prediction method, reveals that CgE binds Fc at the C{sub H}2-C{sub H}3 interface, the binding site for several mammalian and bacterial Fc-binding proteins. The structure identifies interface histidines that may confer pH-dependent binding and regions of CgE implicated in cell-to-cell spread of virus. The ternary organization of the gE-gI/Fc complex is compatible with antibody bipolar bridging, which can interfere with the antiviral immune response.« less
  • The synthesis of hemoglobin A (HbA) is exquisitely coordinated during erythrocyte development to prevent damaging effects from individual {alpha}- and {beta}-subunits. The {alpha}-hemoglobin-stabilizing protein (AHSP) binds {alpha}-hemoglobin ({alpha}Hb), inhibits the ability of {alpha}Hb to generate reactive oxygen species and prevents its precipitation on exposure to oxidant stress. The structure of AHSP bound to ferrous {alpha}Hb is thought to represent a transitional complex through which {alpha}Hb is converted to a non-reactive, hexacoordinate ferric form. Here we report the crystal structure of this ferric {alpha}Hb-AHSP complex at 2.4 Angstrom resolution. Our findings reveal a striking bis-histidyl configuration in which both the proximalmore » and the distal histidines coordinate the haem iron atom. To attain this unusual conformation, segments of {alpha}Hb undergo drastic structural rearrangements, including the repositioning of several {alpha}-helices. Moreover, conversion to the ferric bis-histidine configuration strongly and specifically inhibits redox chemistry catalysis and haem loss from {alpha}Hb. The observed structural changes, which impair the chemical reactivity of haem iron, explain how AHSP stabilizes {alpha}Hb and prevents its damaging effects in cells.« less
  • GTP cyclohydrolase (GCH) III from Methanocaldococcus jannaschii, which catalyzes the conversion of GTP to 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (FAPy), has been shown to require Mg{sup 2+} for catalytic activity and is activated by monovalent cations such as K{sup +} and ammonium [Graham, D. E., Xu, H., and White, R. H. (2002) Biochemistry 41, 15074-15084]. The reaction is formally identical to that catalyzed by a GCH II ortholog (SCO 6655) from Streptomyces coelicolor; however, SCO 6655, like other GCH II proteins, is a zinc-containing protein. The structure of GCH III complexed with GTP solved at 2 {angstrom} resolution clearly shows that GCH IIImore » adopts a distinct fold that is closely related to the palm domains of phosphodiesterases, such as DNA polymerase I. GCH III is a tetramer of identical subunits; each monomer is composed of an N- and a C-terminal domain that adopt nearly superimposible structures, suggesting that the protein has arisen by gene duplication. Three metal ions were located in the active site, two of which occupy positions that are analogous to those occupied by divalent metal ions in the structures of a number of palm domain containing proteins, such as DNA polymerase I. Two conserved Asp residues that coordinate the metal ions, which are also found in palm domain containing proteins, are observed in GCH III. Site-directed variants (Asp{yields}Asn) of these residues in GCH III are less active than wild-type. The third metal ion, most likely a potassium ion, is involved in substrate recognition through coordination of O6 of GTP. The arrangement of the metal ions in the active site suggests that GCH III utilizes two metal ion catalysis. The structure of GCH III extends the repertoire of possible reactions with a palm fold to include cyclohydrolase chemistry.« less